{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T09:35:55Z","timestamp":1790760955991,"version":"4.1.0"},"reference-count":49,"publisher":"Elsevier BV","issue":"49","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,1,13]],"date-time":"2021-01-13T00:00:00Z","timestamp":1610496000000},"content-version":"vor","delay-in-days":43,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002803","name":"Fondazione Cariplo","doi-asserted-by":"publisher","award":["2015-0591"],"award-info":[{"award-number":["2015-0591"]}],"id":[{"id":"10.13039\/501100002803","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002803","name":"Fondazione Cariplo","doi-asserted-by":"publisher","award":["2016-0489"],"award-info":[{"award-number":["2016-0489"]}],"id":[{"id":"10.13039\/501100002803","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005010","name":"Associazione Italiana per la Ricerca sul Cancro","doi-asserted-by":"publisher","award":["9965"],"award-info":[{"award-number":["9965"]}],"id":[{"id":"10.13039\/501100005010","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003196","name":"Ministero della Salute","doi-asserted-by":"publisher","award":["RF-2013-02355259"],"award-info":[{"award-number":["RF-2013-02355259"]}],"id":[{"id":"10.13039\/501100003196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003196","name":"Ministero della Salute","doi-asserted-by":"publisher","award":["RF-2016-02361756"],"award-info":[{"award-number":["RF-2016-02361756"]}],"id":[{"id":"10.13039\/501100003196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003197","name":"Ministry of Health, Italy | Agenzia Italiana del Farmaco, Ministero della Salute","doi-asserted-by":"publisher","award":["AIFA-2016-02364602"],"award-info":[{"award-number":["AIFA-2016-02364602"]}],"id":[{"id":"10.13039\/501100003197","id-type":"DOI","asserted-by":"publisher"}]},{"name":"EUROPEAN JOINT PROGRAMME ON RARE DISEASES","award":["E-RARE JTC 2016 grant ReDox"],"award-info":[{"award-number":["E-RARE JTC 2016 grant ReDox"]}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2020,12]]},"DOI":"10.1074\/jbc.ra120.013461","type":"journal-article","created":{"date-parts":[[2020,9,21]],"date-time":"2020-09-21T01:45:11Z","timestamp":1600652711000},"page":"16572-16584","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":64,"title":["Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis"],"prefix":"10.1016","volume":"295","author":[{"given":"Francesca","family":"Lavatelli","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giulia","family":"Mazzini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6678-5873","authenticated-orcid":false,"given":"Stefano","family":"Ricagno","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Federica","family":"Iavarone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6350-1919","authenticated-orcid":false,"given":"Paola","family":"Rognoni","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paolo","family":"Milani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mario","family":"Nuvolone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paolo","family":"Swuec","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Serena","family":"Caminito","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masayoshi","family":"Tasaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3287-9024","authenticated-orcid":false,"given":"Antonio","family":"Chaves-Sanjuan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Urbani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giampaolo","family":"Merlini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giovanni","family":"Palladini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.013461_bib1","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1080\/13506129.2018.1549825","article-title":"Amyloid nomenclature 2018: recommendations by the International Society of Amyloidosis (ISA) nomenclature committee","volume":"25","author":"Benson","year":"2018","journal-title":"Amyloid"},{"key":"10.1074\/jbc.RA120.013461_bib2","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.1073\/pnas.87.7.2843","article-title":"Fibril in senile systemic amyloidosis is derived from normal transthyretin","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1074\/jbc.RA120.013461_bib3","first-page":"703","article-title":"Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis","volume":"73","author":"Gustavsson","year":"1995","journal-title":"Lab. Invest"},{"key":"10.1074\/jbc.RA120.013461_bib4","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/path.1759","article-title":"Amyloid deposits in transthyretin-derived amyloidosis: cleaved transthyretin is associated with distinct amyloid morphology","volume":"206","author":"Bergstr\u00f6m","year":"2005","journal-title":"J. Pathol"},{"key":"10.1074\/jbc.RA120.013461_bib5","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1021\/ac061546s","article-title":"Detailed structural analysis of amyloidogenic wild-type transthyretin using a novel purification strategy and mass spectrometry","volume":"79","author":"Kingsbury","year":"2007","journal-title":"Anal. Chem"},{"key":"10.1074\/jbc.RA120.013461_bib6","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1002\/path.2607","article-title":"Fibril protein fragmentation pattern in systemic AL-amyloidosis","volume":"219","author":"Enqvist","year":"2009","journal-title":"J. Pathol"},{"key":"10.1074\/jbc.RA120.013461_bib7","doi-asserted-by":"crossref","first-page":"1570","DOI":"10.1074\/mcp.M700545-MCP200","article-title":"Amyloidogenic and associated proteins in systemic amyloidosis proteome of adipose tissue","volume":"7","author":"Lavatelli","year":"2008","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.RA120.013461_bib8","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.bbapap.2005.07.019","article-title":"Proteomics of \u03b22-microglobulin amyloid fibrils","volume":"1753","author":"Stoppini","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA120.013461_bib9","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/S0002-9440(10)65167-X","article-title":"The new apolipoprotein A-I variant Leu174 \u2192 Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide","volume":"155","author":"Obici","year":"1999","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.RA120.013461_bib10","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1152\/physrev.00023.2009","article-title":"Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process","volume":"90","author":"De Strooper","year":"2010","journal-title":"Physiol. Rev"},{"key":"10.1074\/jbc.RA120.013461_bib11","doi-asserted-by":"crossref","first-page":"14192","DOI":"10.1074\/jbc.RA118.003990","article-title":"Plasminogen activation triggers transthyretin amyloidogenesis","volume":"293","author":"Mangione","year":"2018","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013461_bib12","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.15252\/emmm.201505357","article-title":"A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis","volume":"7","author":"Marcoux","year":"2015","journal-title":"EMBO Mol. Med"},{"key":"10.1074\/jbc.RA120.013461_bib13","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1006\/jsbi.2000.4248","article-title":"Review: immunoglobulin light chain amyloidosis\u2013the archetype of structural and pathogenic variability","volume":"130","author":"Bellotti","year":"2000","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.RA120.013461_bib14","doi-asserted-by":"crossref","first-page":"19659","DOI":"10.1074\/jbc.RA118.004142","article-title":"Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light-chain amyloidosis","volume":"293","author":"Brumshtein","year":"2018","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013461_bib15","doi-asserted-by":"crossref","first-page":"27513","DOI":"10.1074\/jbc.M114.585638","article-title":"Formation of amyloid fibers by monomeric light chain variable domains","volume":"289","author":"Brumshtein","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013461_bib16","doi-asserted-by":"crossref","first-page":"4280","DOI":"10.1016\/j.jmb.2016.08.021","article-title":"The kinetic stability of a full-length antibody light chain dimer determines whether endoproteolysis can release amyloidogenic variable domains","volume":"428","author":"Morgan","year":"2016","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013461_bib17","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-09133-w","article-title":"Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient","volume":"10","author":"Swuec","year":"2019","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA120.013461_bib18","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-09032-0","article-title":"Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis","volume":"10","author":"Radamaker","year":"2019","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA120.013461_bib19","doi-asserted-by":"crossref","first-page":"4957","DOI":"10.1182\/blood-2009-07-230722","article-title":"Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens","volume":"114","author":"Vrana","year":"2009","journal-title":"Blood"},{"key":"10.1074\/jbc.RA120.013461_bib20","doi-asserted-by":"crossref","first-page":"9848","DOI":"10.1021\/bi101351c","article-title":"The critical role of the constant region in thermal stability and aggregation of amyloidogenic immunoglobulin light chain","volume":"49","author":"Klimtchuk","year":"2010","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013461_bib21","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1006\/bbrc.1998.9508","article-title":"Fragments of the constant region of immunoglobulin light chains are constituents of AL-amyloid proteins","volume":"251","author":"Olsen","year":"1998","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/jbc.RA120.013461_bib22","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1002\/path.1553","article-title":"Cleavage of AL amyloid proteins and AL amyloid deposits by cathepsins B, K, and L","volume":"203","author":"Bohne","year":"2004","journal-title":"J. Pathol"},{"key":"10.1074\/jbc.RA120.013461_bib23","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1016\/S0002-9440(10)64050-3","article-title":"A putative role for cathepsin K in degradation of AA and AL amyloidosis","volume":"158","author":"R\u00f6cken","year":"2001","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.RA120.013461_bib24","doi-asserted-by":"crossref","first-page":"8360","DOI":"10.1073\/pnas.1817567116","article-title":"Stabilization of amyloidogenic immunoglobulin light chains by small molecules","volume":"116","author":"Morgan","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1074\/jbc.RA120.013461_bib25","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1515\/bchm3.1992.373.2.629","article-title":"Amyloid formation from immunoglobulin chains","volume":"373","author":"Eulitz","year":"1992","journal-title":"Biol. Chem. Hoppe Seyler"},{"key":"10.1074\/jbc.RA120.013461_bib26","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-16953-7","article-title":"Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity","volume":"7","author":"Oberti","year":"2017","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.RA120.013461_bib27","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1172\/JCI105784","article-title":"The characterization of soluble amyloid prepared in water","volume":"47","author":"Pras","year":"1968","journal-title":"J. Clin. Invest"},{"key":"10.1074\/jbc.RA120.013461_bib28","doi-asserted-by":"crossref","first-page":"5642","DOI":"10.1021\/pr400583h","article-title":"Shotgun protein profile of human adipose tissue and its changes in relation to systemic amyloidoses","volume":"12","author":"Brambilla","year":"2013","journal-title":"J. Proteome Res"},{"key":"10.1074\/jbc.RA120.013461_bib29","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-11296-9","article-title":"N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen","volume":"7","author":"Berry","year":"2017","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.RA120.013461_bib30","doi-asserted-by":"crossref","first-page":"2547","DOI":"10.1002\/pmic.201500043","article-title":"The path of no return\u2013Truncated protein N-termini and current ignorance of their genesis","volume":"15","author":"Fortelny","year":"2015","journal-title":"Proteomics"},{"key":"10.1074\/jbc.RA120.013461_bib31","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1002\/pmic.201400301","article-title":"C-terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C-termini","volume":"15","author":"Tanco","year":"2015","journal-title":"Proteomics"},{"key":"10.1074\/jbc.RA120.013461_bib32","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1021\/bi301313b","article-title":"Age-related oxidative modifications of transthyretin modulate its amyloidogenicity","volume":"52","author":"Zhao","year":"2013","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013461_bib33","doi-asserted-by":"crossref","first-page":"5400","DOI":"10.1111\/j.1742-4658.2006.05532.x","article-title":"Oxidation inhibits amyloid fibril formation of transthyretin","volume":"273","author":"Maleknia","year":"2006","journal-title":"FEBS J"},{"key":"10.1074\/jbc.RA120.013461_bib34","doi-asserted-by":"crossref","first-page":"12658","DOI":"10.1021\/ja3039486","article-title":"Deamidation accelerates amyloid formation and alters amylin fiber structure","volume":"134","author":"Dunkelberger","year":"2012","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA120.013461_bib35","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1038\/s41375-018-0194-x","article-title":"Assay to rapidly screen for immunoglobulin light chain glycosylation: a potential path to earlier AL diagnosis for a subset of patients","volume":"33","author":"Kumar","year":"2019","journal-title":"Leukemia"},{"key":"10.1074\/jbc.RA120.013461_bib36","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1136\/ard.2004.030429","article-title":"Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation","volume":"64","author":"R\u00f6cken","year":"2005","journal-title":"Ann. Rheum. Dis"},{"key":"10.1074\/jbc.RA120.013461_bib37","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1002\/path.2076","article-title":"Cathepsin protease activity modulates amyloid load in extracerebral amyloidosis","volume":"210","author":"R\u00f6cken","year":"2006","journal-title":"J. Pathol"},{"key":"10.1074\/jbc.RA120.013461_bib38","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1016\/j.jmb.2019.12.015","article-title":"Inherent biophysical properties modulate the toxicity of soluble amyloidogenic light chains","volume":"432","author":"Maritan","year":"2019","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013461_bib39","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1111\/j.1365-2141.1990.tb02539.x","article-title":"Relevance of class, molecular weight and isoelectric point in predicting human light chain amyloidogenicity","volume":"74","author":"Bellotti","year":"1990","journal-title":"Br. J. Haematol"},{"key":"10.1074\/jbc.RA120.013461_bib40","doi-asserted-by":"crossref","first-page":"77","DOI":"10.3109\/13506129909007307","article-title":"Structural analysis of the amyloidogenic kappa Bence Jones protein (FUR)","volume":"6","author":"Odani","year":"1999","journal-title":"Amyloid"},{"key":"10.1074\/jbc.RA120.013461_bib41","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1182\/blood.V86.3.855.855","article-title":"New drug therapy of amyloidoses: resorption of AL-type deposits with 4\u2032-iodo-4\u2032-deoxydoxorubicin","volume":"86","author":"Gianni","year":"1995","journal-title":"Blood"},{"key":"10.1074\/jbc.RA120.013461_bib42","doi-asserted-by":"crossref","first-page":"7510","DOI":"10.1002\/anie.201701761","article-title":"Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo","volume":"56","author":"Annamalai","year":"2017","journal-title":"Angew Chem Int Ed Engl"},{"key":"10.1074\/jbc.RA120.013461_bib43","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/path.2411","article-title":"Amyloid fibril composition is related to the phenotype of hereditary transthyretin V30M amyloidosis","volume":"216","author":"Ihse","year":"2008","journal-title":"J Pathol"},{"key":"10.1074\/jbc.RA120.013461_bib44","doi-asserted-by":"crossref","first-page":"4822","DOI":"10.1002\/anie.201511524","article-title":"Polymorphism of Amyloid Fibrils In Vivo","volume":"55","author":"Annamalai","year":"2016","journal-title":"Angew. Chem. Int. Ed. Engl"},{"key":"10.1074\/jbc.RA120.013461_bib45","doi-asserted-by":"crossref","first-page":"2954","DOI":"10.1021\/acs.jproteome.9b00264","article-title":"Combination of SCX fractionation and charge-reversal derivatization facilitates the identification of nontryptic peptides in C-terminomics","volume":"18","author":"Kaleja","year":"2019","journal-title":"J. Proteome Res"},{"key":"10.1074\/jbc.RA120.013461_bib46","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1021\/acs.jproteome.6b00146","article-title":"C-terminal charge-reversal derivatization and parallel use of multiple proteases facilitates identification of protein C-termini by C-terminomics","volume":"15","author":"Somasundaram","year":"2016","journal-title":"J. Proteome Res"},{"key":"10.1074\/jbc.RA120.013461_bib47","doi-asserted-by":"crossref","first-page":"D624","DOI":"10.1093\/nar\/gkx1134","article-title":"The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database","volume":"46","author":"Rawlings","year":"2018","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA120.013461_bib48","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: improving support for quantification data","volume":"47","author":"Perez-Riverol","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA120.013461_bib49","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817504767?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817504767?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.013461","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,18]],"date-time":"2021-12-18T06:00:45Z","timestamp":1639807245000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925817504767"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12]]},"references-count":49,"journal-issue":{"issue":"49","published-print":{"date-parts":[[2020,12]]}},"alternative-id":["S0021925817504767"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.013461","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2020,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.013461","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Lavatelli et al.","name":"copyright","label":"Copyright"}]}}